We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1lb3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1lb3.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1lb3.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1lb3| PDB=1lb3 | SCENE= }}
{{STRUCTURE_1lb3| PDB=1lb3 | SCENE= }}
-
'''Structure of recombinant mouse L chain ferritin at 1.2 A resolution'''
+
===Structure of recombinant mouse L chain ferritin at 1.2 A resolution===
-
==Overview==
+
<!--
-
The first ferritin structure refined at the atomic level has been achieved on recombinant mouse L-chain apoferritin (rMoLF) crystals. These latter diffract to 1.2 A resolution under cryogenic conditions. When cryo-cooling the sample, the thermal disorder usually observed at room temperature is reduced and the low-temperature structure reveals several details concerning the protein putative active sites and their properties. Within the pores built up by the molecular three-fold symmetry axes, the iron entry route to the ferritin cavity, residues H118, D131 and E134, exhibit alternate conformations associated with the binding of partially hydrated cadmium ions, a metal used as a crystallization agent. At the mineral ferrihydrite nucleation center, the electron density maps evidence the orientation of E57, E60, E61 and E64 glutamate side chains (whereas they were observed highly disordered in previous ferritin structures determined at room temperature) and allow a description of the site taking into account the binding geometry of four Cd(2+) ions. Moreover, the side chain of residue K140, lying in the vicinity of the ferrihydrite nucleation center, is shown to interact with residue E61. As previously highlighted, this observation confirms the importance of K140 in the rMoLF sequence, as being responsible for the low level of iron incorporation by mousel L-chain ferritin compared to human L-chain ferritin. Finally, the diffusion of small molecules within the ferritin cavity is illustrated here by the presence of ordered molecules of glycerol used as a cryo-protectant, which bind the inner cavity surface of the protein.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12459904}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12459904 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12459904}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Santambrogio, P.]]
[[Category: Santambrogio, P.]]
[[Category: Iron storage]]
[[Category: Iron storage]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:44:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 12:11:24 2008''

Revision as of 09:11, 2 July 2008

Image:1lb3.png

Template:STRUCTURE 1lb3

Structure of recombinant mouse L chain ferritin at 1.2 A resolution

Template:ABSTRACT PUBMED 12459904

About this Structure

1LB3 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structural description of the active sites of mouse L-chain ferritin at 1.2 A resolution., Granier T, Langlois d'Estaintot B, Gallois B, Chevalier JM, Precigoux G, Santambrogio P, Arosio P, J Biol Inorg Chem. 2003 Jan;8(1-2):105-11. Epub 2002 Sep 6. PMID:12459904

Page seeded by OCA on Wed Jul 2 12:11:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lb3"
Personal tools